GenomeNet

Database: UniProt
Entry: A0A1Y1RZ93_9SPIO
LinkDB: A0A1Y1RZ93_9SPIO
Original site: A0A1Y1RZ93_9SPIO 
ID   A0A1Y1RZ93_9SPIO        Unreviewed;       237 AA.
AC   A0A1Y1RZ93;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE            Short=DERA {ECO:0000256|HAMAP-Rule:MF_00114};
DE            EC=4.1.2.4 {ECO:0000256|HAMAP-Rule:MF_00114};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE            Short=Deoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
GN   Name=deoC {ECO:0000256|HAMAP-Rule:MF_00114};
GN   ORFNames=B4O97_07880 {ECO:0000313|EMBL:ORC35979.1};
OS   Marispirochaeta aestuarii.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Marispirochaeta.
OX   NCBI_TaxID=1963862 {ECO:0000313|EMBL:ORC35979.1, ECO:0000313|Proteomes:UP000192343};
RN   [1] {ECO:0000313|EMBL:ORC35979.1, ECO:0000313|Proteomes:UP000192343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC444 {ECO:0000313|EMBL:ORC35979.1,
RC   ECO:0000313|Proteomes:UP000192343};
RA   Shivani Y., Subhash Y., Sasikala C., Ramana C.;
RT   "Draft Genome sequence of Marispirochaeta sp. strain JC444.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC       and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC         3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000764, ECO:0000256|HAMAP-
CC         Rule:MF_00114};
CC   -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC       degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC       deoxy-alpha-D-ribose 1-phosphate: step 2/2. {ECO:0000256|HAMAP-
CC       Rule:MF_00114}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00114}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00010936, ECO:0000256|HAMAP-
CC       Rule:MF_00114}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORC35979.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MWQY01000007; ORC35979.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1RZ93; -.
DR   STRING; 1963862.B4O97_07880; -.
DR   OrthoDB; 9778711at2; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000192343; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00959; DeoC; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00114; DeoC_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR028581; DeoC_typeI.
DR   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889:SF1; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00114};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00114};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192343};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT   ACT_SITE        104
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT   ACT_SITE        168
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT   ACT_SITE        197
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   237 AA;  25242 MW;  6A6BF815D5B9A65A CRC64;
     MKLLTNSAED LQTIRKICSI LDYSGALVPN ATAGMVRKAC EEAQRMKYAA VPVFPAYIPM
     VAEELKGTGI APQVVVGFPS GGARTSVKVK EAEQGIVDGA GEIDMVINIG FLVDGEYKKA
     EEDIRAVVDV AKSADVTVKV IIETGFLSDI DKIEAVEVIC NAGADFVKTC TGFAEGKATV
     HDISLLHQRA KGRIKVKASG GVWTLEDAAA FIEAGAERVA GRYSITHQLE MLGIDRL
//
DBGET integrated database retrieval system